Crystallization and preliminary diffraction analysis of a truncated homodimer of human phenylalanine hydroxylase

被引:17
作者
Erlandsen, H
Martinez, A
Knappskog, PM
Haavik, J
Hough, E
Flatmark, T
机构
[1] UNIV TROMSO, INST MATH & PHYS SCI, PROT CRYSTALLOG GRP, DEPT CHEM, N-9001 TROMSO, NORWAY
[2] UNIV BERGEN, DEPT BIOCHEM & MOL BIOL, BERGEN, NORWAY
[3] UNIV BERGEN, DEPT MED GENET, BERGEN, NORWAY
关键词
phenylalanine hydroxylase; recombinant enzyme; truncated form; crystallization; X-ray diffraction analysis;
D O I
10.1016/S0014-5793(97)00259-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A recombinant truncated form (Delta 1-102/Delta 428-452) of the non-heme iron-dependent metalloenzyme human phenylalanine hydroxylase (hPAH, phenylalanine 4-monooxygenase; EC 1.14.16.1) was expressed in E. coli, purified to homogeneity as a homodimer (70 kDa) and crystallized using the hanging drop vapour diffusion method, The crystals are orthorhombic, space group C222 with cell. dimensions of a=66.6 Angstrom, b=108.4 Angstrom, c=125.7 Angstrom. The calculated packing parameter (V-m) is 3.24 Angstrom(3)/Da with four 2-fold symmetric dimers (or eight momomers) in the unit cell, Data have been collected to 2.0 Angstrom resolution. (C) 1997 Federation of European Biochemical Societies.
引用
收藏
页码:171 / 174
页数:4
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